ID A0A0M4RNG5_9MICC Unreviewed; 262 AA.
AC A0A0M4RNG5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 02-DEC-2020, entry version 28.
DE RecName: Full=Cytochrome bc1 complex cytochrome c subunit {ECO:0000256|ARBA:ARBA00017819, ECO:0000256|PIRNR:PIRNR000007};
DE EC=7.1.1.8 {ECO:0000256|ARBA:ARBA00012951, ECO:0000256|PIRNR:PIRNR000007};
GN ORFNames=AOC05_07200 {ECO:0000313|EMBL:ALE92171.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE92171.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [Fe(III)cytochrome c](out) + a quinol = 2 [Fe(II)cytochrome
CC c](out) + a quinone + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001584,
CC ECO:0000256|PIRNR:PIRNR000007};
CC -!- SUBUNIT: The cytochrome bc1 complex is composed of a cytochrome b
CC (QcrB), the Rieske iron-sulfur protein (QcrA) and a diheme cytochrome c
CC (QcrC) subunit. {ECO:0000256|PIRNR:PIRNR000007}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR000007};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR000007}.
CC -!- PTM: Binds 2 heme groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000007-50}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PIRNR:PIRNR000007}.
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DR EMBL; CP012677; ALE92171.1; -; Genomic_DNA.
DR RefSeq; WP_062006652.1; NZ_CP012677.1.
DR SMR; A0A0M4RNG5; -.
DR EnsemblBacteria; ALE92171; ALE92171; AOC05_07200.
DR KEGG; aaq:AOC05_07200; -.
DR PATRIC; fig|656366.3.peg.1543; -.
DR OrthoDB; 1469969at2; -.
DR Proteomes; UP000062833; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009152; bc1_cytC-su.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR029490; Cytochrom_C550.
DR Pfam; PF14495; Cytochrom_C550; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000007; Ubiq_cycred_cyc; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000007};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000007};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000007,
KW ECO:0000256|PIRSR:PIRSR000007-50, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000007,
KW ECO:0000256|PIRSR:PIRSR000007-51, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Lyase {ECO:0000313|EMBL:ALE92171.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR000007};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000007, ECO:0000256|PIRSR:PIRSR000007-51,
KW ECO:0000256|PROSITE-ProRule:PRU00433};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Reference proteome {ECO:0000313|Proteomes:UP000062833};
KW Respiratory chain {ECO:0000256|PIRNR:PIRNR000007};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000007};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR000007};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR000007};
KW Transport {ECO:0000256|PIRNR:PIRNR000007}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..262
FT /note="Cytochrome bc1 complex cytochrome c subunit"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005801082"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR000007"
FT DOMAIN 48..127
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 142..220
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT METAL 65
FT /note="Iron (heme 1 axial ligand)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-51"
FT METAL 159
FT /note="Iron (heme 2 axial ligand)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-51"
FT BINDING 61
FT /note="Heme 1 (covalent)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 64
FT /note="Heme 1 (covalent)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 155
FT /note="Heme 2 (covalent)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
FT BINDING 158
FT /note="Heme 2 (covalent)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000007-50"
SQ SEQUENCE 262 AA; 27039 MW; DACC559F826167D0 CRC64;
MKALSQKRRH PLAALALLVL GLMLTGGLYA VVTTVNEAKA DTTTFTAQQV EEGEKLFVAN
CATCHGVGAS GTDAGPSLAG VGAAAVDFQV GTGRMPMQMQ GPQARQKPKQ FNADQTRELS
AYVATLGDGP ALPEEQFIDG KGNAAAGGEL FRVNCAMCHN AAAAGGALTR GKFAPALAGV
SNSHMYSAMV TGPQNMPVFN DANISPEGKR DIITFLNTIE NQGSPGGAKL GSLGPVSEGL
FLWTAVMGVV IGFTIWLTSR PS
//
